ID Q6CJT1_KLULA Unreviewed; 596 AA.
AC Q6CJT1;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 2.
DT 24-JAN-2024, entry version 117.
DE RecName: Full=precorrin-2 dehydrogenase {ECO:0000256|ARBA:ARBA00012400};
DE EC=1.3.1.76 {ECO:0000256|ARBA:ARBA00012400};
GN ORFNames=KLLA0_F16170g {ECO:0000313|EMBL:CAG98516.2};
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590 {ECO:0000313|EMBL:CAG98516.2, ECO:0000313|Proteomes:UP000000598};
RN [1] {ECO:0000313|EMBL:CAG98516.2, ECO:0000313|Proteomes:UP000000598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC WM37 {ECO:0000313|Proteomes:UP000000598};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000256|RuleBase:RU003960}.
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DR EMBL; CR382126; CAG98516.2; -; Genomic_DNA.
DR RefSeq; XP_455808.2; XM_455808.2.
DR AlphaFoldDB; Q6CJT1; -.
DR STRING; 284590.Q6CJT1; -.
DR PaxDb; 284590-Q6CJT1; -.
DR GeneID; 2895678; -.
DR KEGG; kla:KLLA0_F16170g; -.
DR eggNOG; KOG1527; Eukaryota.
DR HOGENOM; CLU_011276_2_2_1; -.
DR InParanoid; Q6CJT1; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0019354; P:siroheme biosynthetic process; IEA:InterPro.
DR GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR CDD; cd11642; SUMT; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000878; 4pyrrol_Mease.
DR InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR InterPro; IPR006366; CobA/CysG_C.
DR InterPro; IPR012066; Met1_fungi.
DR InterPro; IPR028281; Sirohaem_synthase_central.
DR InterPro; IPR003043; Uropor_MeTrfase_CS.
DR PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR PANTHER; PTHR45790:SF6; UROPORPHYRINOGEN-III C-METHYLTRANSFERASE; 1.
DR Pfam; PF14824; Sirohm_synth_M; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF036555; SUMT_yeast; 1.
DR SUPFAM; SSF75615; Siroheme synthase middle domains-like; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR PROSITE; PS00839; SUMT_1; 1.
DR PROSITE; PS00840; SUMT_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU003960}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000000598};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT DOMAIN 154..178
FT /note="Siroheme synthase central"
FT /evidence="ECO:0000259|Pfam:PF14824"
FT DOMAIN 330..537
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT REGION 283..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 66463 MW; 075DB5F3C5D1C3FB CRC64;
MSVQNESRFI EKRFTPLITS LKSVGEQYLL IGTHSINVTQ SRISSILDSG ASCVVIHSGK
NSDLKQLSQR FYGNNDVVLL DREFQLSDLT TLGRVAVGKI VDRVFVNLDS KQSLLIRDIF
EQCQKLRIPI NTHQRPEYST FSICSTYNDP GQSGLQIAIT TNGQGCLLAN RIKREIVSRL
PQNISKVVSN MGHLRERIIY EDHNQIIHSH FLNKDLQDLG FGIDEDVWES HKLNKLVYEF
NVSEKQLKMK RSRWLSQIME YYPLQSLAEL SVDQLADQYH KISQEDNSKE NASKKQRNTP
DKKASNVNDA DVQVSTTASS ILDVPKKGSI SLVGSGPGSV SMLTIGALHE IKTADLILAD
KLVPEKVLQL IPQGTETFIA RKFPGNAERA QEELLEKGFD GLQKGLKVVR LKQGDPYIFG
RGGEEFLFFQ DKGYTPLVLP GLSSALAATV VSNIPATQRD VADQVLICTG TGRKGALPNI
PEYVETRTTV FLMSLHRAQV LIDALLEKGW DENVPAAIVE RASCPDQRIT RTLLKNIPQT
VEEIGSRPPG LLVVGNAINV LTDPELLKYD SSNTYHIEEG YEHVGFEDNV QKLLNI
//